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Database: UniProt
Entry: Q87KE0
LinkDB: Q87KE0
Original site: Q87KE0 
ID   PURK_VIBPA              Reviewed;         377 AA.
AC   Q87KE0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   13-FEB-2019, entry version 94.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE            Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE            EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928};
GN   Name=purK {ECO:0000255|HAMAP-Rule:MF_01928}; OrderedLocusNames=VP3037;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC         hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-
CC         ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01928};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01928}.
DR   EMBL; BA000031; BAC61300.1; -; Genomic_DNA.
DR   RefSeq; NP_799416.1; NC_004603.1.
DR   RefSeq; WP_005461432.1; NC_004603.1.
DR   ProteinModelPortal; Q87KE0; -.
DR   SMR; Q87KE0; -.
DR   STRING; 223926.VP3037; -.
DR   EnsemblBacteria; BAC61300; BAC61300; BAC61300.
DR   GeneID; 1190636; -.
DR   KEGG; vpa:VP3037; -.
DR   PATRIC; fig|223926.6.peg.2921; -.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034026; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   BioCyc; VPAR223926:G1GTB-3179-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    377       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000075017.
FT   DOMAIN       97    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     138    144       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     175    178       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     257    258       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING      93     93       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     133    133       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     183    183       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     206    206       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   377 AA;  41049 MW;  977C1551533246C4 CRC64;
     MHVLVLGSGQ LARMMSLAGA PLNIQISAYD VGSGNVVHPL TQQVLGHGLE NAIEQVDAIT
     AEFEHIPHDV LDICELSGKF LPSTAAIKAG GDRRVEKALL DNAGVRNAKH YVIETREDFE
     RAIEHVGIPM VLKSALGGYD GKGQWRLKEA AQIETIWAEM AECIAATPTQ AIVAEEFVPF
     NREVSLVGAR GKDGSVEVYP LAENVHTNGV LSLSTAIDAP ELQAQAKQMF TAVADSLNYV
     GVLALEFFDV EGTLLVNEIA PRVHNSGHWT QQGAETCQFE NHLRAVCGLP LGSTKLIRET
     SMVNILGEDT LPEALLAMDG CHIHWYGKEK REGRKMGHIN VCGDYPGELH RRLCALAEVL
     DPMIFPAVHE FAKQAQR
//
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